info:eu-repo/semantics/article
Inhibition pattern of sulfamide-related compounds in binding to carbonic anhydrase isoforms I, II, VII, XII and XIV
Fecha
2013-03Registro en:
Gavernet, Luciana; González Funes, José L.; Palestro, Pablo Hernán; Bruno Blanch, Luis Enrique; Estiu, Guillermina Lucia; et al.; Inhibition pattern of sulfamide-related compounds in binding to carbonic anhydrase isoforms I, II, VII, XII and XIV; Pergamon-Elsevier Science Ltd; Bioorganic & Medicinal Chemistry; 21; 6; 3-2013; 1410-1418
0968-0896
CONICET Digital
CONICET
Autor
Gavernet, Luciana
González Funes, José L.
Palestro, Pablo Hernán
Bruno Blanch, Luis Enrique
Estiu, Guillermina Lucia
Maresca, Alfonso
Barrios, Ivana Analia
Supuran, Claudiu T.
Resumen
A set of sulfamides and sulfamates were synthesized and tested against several isoforms of carbonic anhydrase: CA I, CA II, CA VII, CA XII and CA XIV. The biological assays showed a broad range of inhibitory activity, and interesting results were found for several compounds in terms of activity (Ki <1 μm) and selectivity: some aromatic sulfamides are active against CA I, CA II and/or CA VII; while they are less active in CA XII and CA XIV. On the other hand, bulky sulfamides are selective to CA VII. To understand the origin of the different inhibitory activity against each isozyme we used molecular modeling techniques such as docking and molecular dynamic simulations.